Fundamental aspects of the structural biology of coronaviruses Chapter uri icon

abstract

  • The development of structural tools to study macromolecular complexes has forever changed how we understand viruses, their interactions with the host-cell, small molecules, and antibodies (Dülfer et al., 2019; Jun et al., 2019; Koning et al., 2018; Kuhlman %26 Bradley, 2019; Kurta et al., 2017; Maciejewski et al., 2017; Renaud et al., 2018; Zhang, 2019). In particular, the improvements in cryo-EM made in the last decade have allowed studying viruses with atomic resolution (Strack, 2020) and publishing three-dimensional structures at a formidable rate. In fact, most of the current advances that have been accomplished since the first genome of the SARS-CoV-2 was published would be impossible without cryo-EM. Unfortunately, the structure of some viral proteins has not been solved (e.g., protein M). This can be associated to their physicochemical properties (e.g., highly hydrophobic or extremely disordered tertiary structures), which make their expression and purification extremely challenging. However, by using computational approaches, one can use a known structure of the homologous protein as template to predict the structure of a novel protein (Kuhlman %26 Bradley, 2019; Senior et al., 2020). Furthermore, we can use their three-dimensional structure (and/or predicted structure) to search for small molecules that could have antiviral activity (Schlicksup %26 Zlotnick, 2020). © 2022 Elsevier Inc. All rights reserved.

publication date

  • 2022-01-01